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P10686

- PLCG1_RAT

UniProt

P10686 - PLCG1_RAT

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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.

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 – 3351 By similarity
Active sitei380 – 3801 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi165 – 17612 Reviewed prediction
Add
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. protein binding Source: IntAct
  6. 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.

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 – 11Removed By similarity
Chaini2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
PRO_0000088500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei506 – 5061Phosphotyrosine By similarity
Modified residuei771 – 7711Phosphotyrosine; by SYK By similarity
Modified residuei775 – 7751Phosphotyrosine By similarity
Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK By similarity
Modified residuei977 – 9771Phosphotyrosine By similarity
Modified residuei1221 – 12211Phosphoserine By similarity
Modified residuei1248 – 12481Phosphoserine By similarity
Modified residuei1253 – 12531Phosphotyrosine By 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.1 Publication
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.2 Publications

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP10686.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 142116PH 1
Add
BLAST
Domaini152 – 18736EF-hand
Add
BLAST
Domaini320 – 464145PI-PLC X-box
Add
BLAST
Domaini489 – 52335PH 2; first part
Add
BLAST
Domaini550 – 657108SH2 1
Add
BLAST
Domaini668 – 75689SH2 2
Add
BLAST
Domaini791 – 85161SH3
Add
BLAST
Domaini895 – 93137PH 2; second part
Add
BLAST
Domaini953 – 1070118PI-PLC Y-box
Add
BLAST
Domaini1075 – 1177103C2
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 EF-hand domain.
Contains 2 PH domains.
Contains 2 SH2 domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
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

MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT     50
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP 150
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT GERPELCQVS 250
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 300
FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP 450
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP 500
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSSEKW 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 VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI 850
NPAILEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 900
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA 950
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF 1000
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN 1050
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL 1100
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS 1150
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 1200
ELASLLIKID IFPAKENGDL SPFSGTSLRE RASDASSQLF HVRAREGSFE 1250
ARYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL 1290
Length:1,290
Mass (Da):148,548
Last modified:July 1, 1989 - v1
Checksum:iBB3240C27972CE3B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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.
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.

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: September 3, 2014
This is version 166 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

Similar proteinsi