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Q8CIH5

- PLCG2_MOUSE

UniProt

Q8CIH5 - PLCG2_MOUSE

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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

Gene

Plcg2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling (By similarity).By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei327 – 3271PROSITE-ProRule annotation
Active sitei372 – 3721PROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphatidylinositol phospholipase C activity Source: UniProtKB
  2. phospholipase C activity Source: MGI
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of store-operated calcium channel activity Source: MGI
  2. B cell differentiation Source: UniProtKB
  3. B cell receptor signaling pathway Source: UniProtKB
  4. follicular B cell differentiation Source: MGI
  5. inositol trisphosphate biosynthetic process Source: MGI
  6. intracellular signal transduction Source: InterPro
  7. negative regulation of programmed cell death Source: MGI
  8. phosphatidylinositol biosynthetic process Source: UniProtKB
  9. phospholipid catabolic process Source: InterPro
  10. regulation of gene expression Source: MGI
  11. release of sequestered calcium ion into cytosol Source: UniProtKB
  12. response to lipopolysaccharide Source: MGI
  13. T cell receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188530. FCERI mediated MAPK activation.
REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_220092. GPVI-mediated activation cascade.
REACT_246719. Toll Like Receptor 4 (TLR4) Cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-gamma-2
Phospholipase C-gamma-2
Short name:
PLC-gamma-2
Gene namesi
Name:Plcg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:97616. Plcg2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2PRO_0000342364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei753 – 7531Phosphotyrosine; alternate1 Publication
Modified residuei753 – 7531Phosphotyrosine; by BTK; alternate1 Publication
Modified residuei759 – 7591Phosphotyrosine; by BTKBy similarity
Modified residuei1197 – 11971Phosphotyrosine; by BTKBy similarity
Modified residuei1217 – 12171Phosphotyrosine1 Publication
Modified residuei1245 – 12451Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-induced activation of a variety of growth factor receptors and immune system receptors. Phosphorylation leads to increased phospholipase activity (By similarity). Phosphorylated on tyrosine residues by CSF1R.By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CIH5.
PaxDbiQ8CIH5.
PRIDEiQ8CIH5.

PTM databases

PhosphoSiteiQ8CIH5.

Expressioni

Gene expression databases

BgeeiQ8CIH5.
GenevestigatoriQ8CIH5.

Interactioni

Subunit structurei

Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EporP147532EBI-617954,EBI-617901
Fhl2O704333EBI-617954,EBI-299379
FlnaQ8BTM83EBI-617954,EBI-641991
Fn1P112766EBI-617954,EBI-641955
Inpp5dQ9ES523EBI-617954,EBI-300210
LynP259112EBI-617954,EBI-643537
Pdcd6ipQ9WU787EBI-617954,EBI-641897
Trim27Q621584EBI-617954,EBI-642025
Zbtb7bQ643213EBI-617954,EBI-642868

Protein-protein interaction databases

IntActiQ8CIH5. 32 interactions.
MINTiMINT-1348529.
STRINGi10090.ENSMUSP00000079991.

Structurei

Secondary structure

1
1265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi523 – 5253Combined sources
Helixi540 – 55112Combined sources
Turni552 – 5554Combined sources
Beta strandi561 – 5655Combined sources
Beta strandi567 – 5693Combined sources
Beta strandi573 – 5797Combined sources
Beta strandi582 – 59312Combined sources
Beta strandi596 – 6027Combined sources
Beta strandi607 – 6093Combined sources
Helixi610 – 6167Combined sources
Turni617 – 6193Combined sources
Helixi625 – 6273Combined sources
Beta strandi773 – 7786Combined sources
Beta strandi784 – 7863Combined sources
Beta strandi795 – 7984Combined sources
Beta strandi803 – 8053Combined sources
Beta strandi807 – 8115Combined sources
Beta strandi814 – 8196Combined sources
Helixi821 – 8233Combined sources
Beta strandi824 – 8263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DX0X-ray2.50A/B516-640[»]
2EQINMR-A772-827[»]
ProteinModelPortaliQ8CIH5.
SMRiQ8CIH5. Positions 159-446, 476-511, 520-829, 844-909, 930-1181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CIH5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 131131PHPROSITE-ProRule annotationAdd
BLAST
Domaini312 – 456145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini532 – 635104SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini646 – 73590SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini769 – 82961SH3PROSITE-ProRule annotationAdd
BLAST
Domaini930 – 1044115PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1048 – 1152105C2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PH domain.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.
GeneTreeiENSGT00730000110782.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiQ8CIH5.
KOiK05859.
OMAiMLMRIPR.
OrthoDBiEOG7W419X.
PhylomeDBiQ8CIH5.
TreeFamiTF313216.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
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:SF25. PTHR10336:SF25. 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. 2 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.
PS50003. PH_DOMAIN. 1 hit.
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.

Q8CIH5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTMVNVDTL PEYEKSQIKR ALELGTVMTV FNARKSTPER RTVQMIMETR
60 70 80 90 100
QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRH KAECCFTILY
110 120 130 140 150
GTQFVLSTLS LATDSKEDAV KWLSGLKILH QEAMSASTPT MIESWLRKQI
160 170 180 190 200
YSVDQTRRNS ISLRELKTIL PLVNFKVSGI KFLKDKLVEI GAQKDELSFE
210 220 230 240 250
QFHLFYKKLM FDQQKSILDE FKKDSSVFIL GNTDRPDASA VYLQDFQRFL
260 270 280 290 300
LHEQQELWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS
310 320 330 340 350
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR
360 370 380 390 400
AGCRCIELDC WDGPDGKPII YHGWTRTTKI KFDDVVQAIR DHAFVTSSFP
410 420 430 440 450
VILSIEEHCS VEQQRHMAKV FKEVLGDMLL TKPTEASADQ LPSPSQLREK
460 470 480 490 500
IIIKHKKLGP KGDVDVNVED KKDEHKPQGE LYMWDSIDQK WTRHYCAIAD
510 520 530 540 550
AKLSFGDDIE QAVEEEPVQD TPPTELHFGE KWFHKKVESR TSAEKLLQEY
560 570 580 590 600
CAETGAKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMENGVMKYY
610 620 630 640 650
LTDNLTFNSI YALIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDS
660 670 680 690 700
LSRGEAEDML MRIPRDGAFL IRKREGTNSY AITFRARGKV KHCRINRDGR
710 720 730 740 750
HFVLGTSAYF ESLVELVSYY EKHALYRKMR LRYPVTPELL ERYNMERDIN
760 770 780 790 800
SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELTF CRGALIHNVS
810 820 830 840 850
KEPGGWWKGD YGTRIQQYFP SNYVEDISAG DAEEMEKQII EDNPLGSLCK
860 870 880 890 900
GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF
910 920 930 940 950
QSIREITWKM DTKENNMKYW ERNQSIAIEL SDLVVYCKPT SKTKDHLENP
960 970 980 990 1000
DFREIRSFVE TKADSIVRQK PVDLLRYNQK GLTRVYPKGQ RVDSSNYDPF
1010 1020 1030 1040 1050
RLWLCGSQMV ALNFQTPDKY MQMNHALFSL NGRTGYVLQP ESMRSEKYDP
1060 1070 1080 1090 1100
MPLESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDSNKFK
1110 1120 1130 1140 1150
TTVVNDNGLS PVWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH
1160 1170 1180 1190 1200
ATYPIKGIKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC
1210 1220 1230 1240 1250
RQLRRRQEEL NNQLFLYDTH QNLRGANRDA LVKEFNVNEN QLQLYQEKCN
1260
RRLREKRVSN SRFYS
Length:1,265
Mass (Da):147,592
Last modified:March 1, 2003 - v1
Checksum:iE4A2A6AD6F05160E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti787 – 7871E → G in BAE24959. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK142173 mRNA. Translation: BAE24959.1.
AK151039 mRNA. Translation: BAE30056.1.
BC019654 mRNA. Translation: AAH19654.1.
BC023877 mRNA. Translation: AAH23877.1.
CCDSiCCDS22700.1.
RefSeqiNP_758489.1. NM_172285.1.
UniGeneiMm.192699.

Genome annotation databases

EnsembliENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
GeneIDi234779.
KEGGimmu:234779.
UCSCiuc009npc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK142173 mRNA. Translation: BAE24959.1 .
AK151039 mRNA. Translation: BAE30056.1 .
BC019654 mRNA. Translation: AAH19654.1 .
BC023877 mRNA. Translation: AAH23877.1 .
CCDSi CCDS22700.1.
RefSeqi NP_758489.1. NM_172285.1.
UniGenei Mm.192699.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DX0 X-ray 2.50 A/B 516-640 [» ]
2EQI NMR - A 772-827 [» ]
ProteinModelPortali Q8CIH5.
SMRi Q8CIH5. Positions 159-446, 476-511, 520-829, 844-909, 930-1181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CIH5. 32 interactions.
MINTi MINT-1348529.
STRINGi 10090.ENSMUSP00000079991.

PTM databases

PhosphoSitei Q8CIH5.

Proteomic databases

MaxQBi Q8CIH5.
PaxDbi Q8CIH5.
PRIDEi Q8CIH5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081232 ; ENSMUSP00000079991 ; ENSMUSG00000034330 .
GeneIDi 234779.
KEGGi mmu:234779.
UCSCi uc009npc.1. mouse.

Organism-specific databases

CTDi 5336.
MGIi MGI:97616. Plcg2.

Phylogenomic databases

eggNOGi NOG268751.
GeneTreei ENSGT00730000110782.
HOGENOMi HOG000230864.
HOVERGENi HBG053611.
InParanoidi Q8CIH5.
KOi K05859.
OMAi MLMRIPR.
OrthoDBi EOG7W419X.
PhylomeDBi Q8CIH5.
TreeFami TF313216.

Enzyme and pathway databases

Reactomei REACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188530. FCERI mediated MAPK activation.
REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_220092. GPVI-mediated activation cascade.
REACT_246719. Toll Like Receptor 4 (TLR4) Cascade.

Miscellaneous databases

EvolutionaryTracei Q8CIH5.
NextBioi 382355.
PROi Q8CIH5.
SOURCEi Search...

Gene expression databases

Bgeei Q8CIH5.
Genevestigatori Q8CIH5.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
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:SF25. PTHR10336:SF25. 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. 2 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.
PS50003. PH_DOMAIN. 1 hit.
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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage and Embryonic heart.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  3. "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
    Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
    EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH CSF1R.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-753; TYR-1217 AND TYR-1245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. "Crystal structure of the N-terminal SH2 domain of mouse phospholipase c-gamma 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 516-640.

Entry informationi

Entry nameiPLCG2_MOUSE
AccessioniPrimary (citable) accession number: Q8CIH5
Secondary accession number(s): Q3UBA8, Q3UQT0, Q8VE69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 113 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3