Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10686

- PLCG1_RAT

UniProt

P10686 - PLCG1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

Plcg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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. insulin receptor binding Source: RGD
  3. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  4. phosphoprotein binding Source: RGD
  5. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. calcium ion transport Source: RGD
  2. cellular response to epidermal growth factor stimulus Source: UniProtKB
  3. inositol trisphosphate biosynthetic process Source: RGD
  4. intracellular signal transduction Source: InterPro
  5. phospholipid catabolic process Source: InterPro
  6. positive regulation of epithelial cell migration Source: RGD
  7. protein secretion Source: RGD
  8. regulation of store-operated calcium channel activity Source: RGD
  9. response to gravity Source: RGD
  10. response to hydrogen peroxide Source: RGD
  11. response to morphine Source: RGD
  12. response to organonitrogen compound Source: RGD
  13. signal transduction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.
ReactomeiREACT_194374. Role of phospholipids in phagocytosis.
REACT_219269. PLC-gamma1 signalling.
REACT_220575. DAG and IP3 signaling.
REACT_242711. Role of second messengers in netrin-1 signaling.
REACT_247187. VEGFR2 mediated cell proliferation.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:Plcg1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3347. Plcg1.

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. cytoplasm Source: RGD
  3. lamellipodium Source: UniProtKB
  4. plasma membrane Source: Reactome
  5. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi842 – 8421P → L: Inhibits interaction with AGAP2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei506 – 5061PhosphotyrosineBy similarity
Modified residuei771 – 7711Phosphotyrosine; by SYKBy similarity
Modified residuei775 – 7751PhosphotyrosineBy similarity
Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXKBy similarity
Modified residuei977 – 9771PhosphotyrosineBy similarity
Modified residuei1221 – 12211PhosphoserineBy similarity
Modified residuei1248 – 12481PhosphoserineBy similarity
Modified residuei1253 – 12531PhosphotyrosineBy similarity

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, KIT and PDGFRB. 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

PaxDbiP10686.
PRIDEiP10686.

PTM databases

PhosphoSiteiP10686.

Miscellaneous databases

PMAP-CutDBP10686.

Expressioni

Gene expression databases

GenevestigatoriP10686.

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 the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT. Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated) (By similarity). 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
FGFR1P113624EBI-520788,EBI-1028277From a different organism.
Fgfr1Q045892EBI-520788,EBI-2480918
Jak2Q621203EBI-520788,EBI-646604From a different organism.
PTPN1P180314EBI-520788,EBI-968788From a different organism.
TRPC3Q135072EBI-520788,EBI-520807From a different organism.

Protein-protein interaction databases

BioGridi247766. 1 interaction.
DIPiDIP-2863N.
IntActiP10686. 10 interactions.
MINTiMINT-231720.
STRINGi10116.ENSRNOP00000022276.

Structurei

Secondary structure

1
1290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi491 – 4999Combined sources
Turni500 – 5034Combined sources
Beta strandi504 – 51310Combined sources
Beta strandi516 – 5194Combined sources
Beta strandi551 – 5533Combined sources
Helixi556 – 5583Combined sources
Helixi561 – 57616Combined sources
Beta strandi583 – 5875Combined sources
Beta strandi589 – 5913Combined sources
Beta strandi594 – 6007Combined sources
Beta strandi605 – 6139Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi620 – 6245Combined sources
Beta strandi627 – 6315Combined sources
Helixi632 – 64110Combined sources
Helixi665 – 6684Combined sources
Beta strandi669 – 6724Combined sources
Helixi675 – 6828Combined sources
Beta strandi690 – 6956Combined sources
Beta strandi701 – 7088Combined sources
Beta strandi711 – 72010Combined sources
Beta strandi723 – 7264Combined sources
Beta strandi729 – 7335Combined sources
Helixi734 – 74310Combined sources
Helixi758 – 7625Combined sources
Beta strandi796 – 8005Combined sources
Beta strandi817 – 8226Combined sources
Beta strandi825 – 8339Combined sources
Beta strandi836 – 8427Combined sources
Helixi843 – 8453Combined sources
Beta strandi846 – 8483Combined sources
Beta strandi860 – 8623Combined sources
Turni864 – 8707Combined sources
Beta strandi874 – 8763Combined sources
Beta strandi882 – 8865Combined sources
Beta strandi890 – 8923Combined sources
Beta strandi896 – 9005Combined sources
Beta strandi904 – 9063Combined sources
Beta strandi909 – 9124Combined sources
Helixi916 – 93015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y0MX-ray1.20A791-851[»]
1YWOX-ray1.81A790-851[»]
1YWPX-ray1.60A790-851[»]
2FJLNMR-A489-547[»]
A851-933[»]
3GQIX-ray2.50B545-770[»]
4K44X-ray1.70A/B664-766[»]
4K45X-ray1.50A664-766[»]
B770-787[»]
ProteinModelPortaliP10686.
SMRiP10686. Positions 320-454, 489-658, 663-759, 795-848, 851-933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10686.

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.
InParanoidiP10686.
KOiK01116.
PhylomeDBiP10686.

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.
PF00169. PH. 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.

P10686-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT GERPELCQVS
260 270 280 290 300
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSSEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI
860 870 880 890 900
NPAILEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGTSLRE RASDASSQLF HVRAREGSFE
1260 1270 1280 1290
ARYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
Length:1,290
Mass (Da):148,548
Last modified:July 1, 1989 - v1
Checksum:iBB3240C27972CE3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03806 mRNA. Translation: AAA41921.1.
L14476 Genomic DNA. No translation available.
PIRiA31317.
RefSeqiNP_037319.1. NM_013187.1.
UniGeneiRn.11243.

Genome annotation databases

GeneIDi25738.
KEGGirno:25738.
UCSCiRGD:3347. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03806 mRNA. Translation: AAA41921.1 .
L14476 Genomic DNA. No translation available.
PIRi A31317.
RefSeqi NP_037319.1. NM_013187.1.
UniGenei Rn.11243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y0M X-ray 1.20 A 791-851 [» ]
1YWO X-ray 1.81 A 790-851 [» ]
1YWP X-ray 1.60 A 790-851 [» ]
2FJL NMR - A 489-547 [» ]
A 851-933 [» ]
3GQI X-ray 2.50 B 545-770 [» ]
4K44 X-ray 1.70 A/B 664-766 [» ]
4K45 X-ray 1.50 A 664-766 [» ]
B 770-787 [» ]
ProteinModelPortali P10686.
SMRi P10686. Positions 320-454, 489-658, 663-759, 795-848, 851-933.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247766. 1 interaction.
DIPi DIP-2863N.
IntActi P10686. 10 interactions.
MINTi MINT-231720.
STRINGi 10116.ENSRNOP00000022276.

Chemistry

BindingDBi P10686.
ChEMBLi CHEMBL5188.

PTM databases

PhosphoSitei P10686.

Proteomic databases

PaxDbi P10686.
PRIDEi P10686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25738.
KEGGi rno:25738.
UCSCi RGD:3347. rat.

Organism-specific databases

CTDi 5335.
RGDi 3347. Plcg1.

Phylogenomic databases

eggNOGi NOG268751.
HOGENOMi HOG000230864.
HOVERGENi HBG053611.
InParanoidi P10686.
KOi K01116.
PhylomeDBi P10686.

Enzyme and pathway databases

BRENDAi 3.1.4.11. 5301.
Reactomei REACT_194374. Role of phospholipids in phagocytosis.
REACT_219269. PLC-gamma1 signalling.
REACT_220575. DAG and IP3 signaling.
REACT_242711. Role of second messengers in netrin-1 signaling.
REACT_247187. VEGFR2 mediated cell proliferation.

Miscellaneous databases

EvolutionaryTracei P10686.
NextBioi 607883.
PMAP-CutDB P10686.
PROi P10686.

Gene expression databases

Genevestigatori P10686.

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.
PF00169. PH. 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. "Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene products."
    Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.
    Proc. Natl. Acad. Sci. U.S.A. 85:5419-5423(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Promoter region of the rat phospholipase C-gamma 1 gene."
    Lee S.J., Ryu S.H., Suh P.G.
    Biochem. Biophys. Res. Commun. 194:294-300(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  3. "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, PHOSPHORYLATION.
  4. "Phospholipase C gamma 1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE."
    Ye K., Aghdasi B., Luo H.R., Moriarity J.L., Wu F.Y., Hong J.J., Hurt K.J., Bae S.S., Suh P.-G., Snyder S.H.
    Nature 415:541-544(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGAP2, MUTAGENESIS OF PRO-842.
  5. "Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3."
    Wen W., Yan J., Zhang M.
    J. Biol. Chem. 281:12060-12068(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 489-553 AND 663-759.

Entry informationi

Entry nameiPLCG1_RAT
AccessioniPrimary (citable) accession number: P10686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 169 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, 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