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

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Q62077 (PLCG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 119. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Plcg1
Synonyms:	Plcg-1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Enzyme regulation	Activated by phosphorylation on tyrosine residues.
Subunit structure	Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET By similarity. Interacts with AGAP2 via its SH3 domain. 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. Interacts with FLT4 and KIT. Interacts with AXL By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19
Subcellular location	Cell projection › lamellipodium By similarity. Cell projection › ruffle By similarity. Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment By similarity.
Domain	The SH3 domain mediates interaction with RALGPS1 By similarity. The SH3 domain also mediates interaction with CLNK. Ref.9
Post-translational modification	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. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ By similarity. Ref.3 Ref.6 Ref.11 Ref.12 Ref.16 Ref.17 Ref.18 Ref.20 Ubiquitinated by CBLB in activated T-cells. Ref.11
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand domain. Contains 2 PH domains. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. Contains 2 SH2 domains. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell projection
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	T cell receptor signaling pathway Inferred from direct assay. Source: MGI cellular response to epidermal growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB in utero embryonic development Inferred from mutant phenotype. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro phospholipid catabolic process Inferred from electronic annotation. Source: InterPro positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro glutamate receptor binding Inferred from physical interaction. Source: MGI phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Epor	P14753	4	EBI-300133,EBI-617901

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 1302

1301

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

PRO_0000088499

Regions

Domain

27 – 142

116

PH 1

Domain

152 – 187

EF-hand

Domain

320 – 464

145

PI-PLC X-box

Domain

489 – 523

PH 2; first part

Domain

550 – 657

108

SH2 1

Domain

668 – 756

SH2 2

Domain

791 – 851

SH3

Domain

895 – 931

PH 2; second part

Domain

953 – 1070

118

PI-PLC Y-box

Domain

1075 – 1177

103

Calcium binding

165 – 176

Potential

Sites

Active site

335

By similarity

Active site

380

By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

379

Phosphotyrosine Ref.17

Modified residue

481

Phosphotyrosine Ref.17

Modified residue

506

Phosphotyrosine Ref.17

Modified residue

525

Phosphoserine By similarity

Modified residue

771

Phosphotyrosine; by SYK

Modified residue

775

Phosphotyrosine Ref.16

Modified residue

783

Phosphotyrosine By similarity

Modified residue

783

Phosphotyrosine; by ITK, SYK and TXK By similarity

Modified residue

977

Phosphotyrosine Ref.17

Modified residue

1221

Phosphoserine By similarity

Modified residue

1248

Phosphoserine Ref.18

Modified residue

1253

Phosphotyrosine By similarity

Modified residue

1263

Phosphoserine Ref.18

Experimental info

Sequence conflict

966

D → A in CAA64639. Ref.2

Sequence conflict

984

P → R in CAA64639. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q62077 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 5D123C508D425EB2
Show »

FASTA

1,302

149,668

        10         20         30         40         50         60 
MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 

        70         80         90        100        110        120 
TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL 

       130        140        150        160        170        180 
SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM 

       190        200        210        220        230        240 
LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT 

       250        260        270        280        290        300 
GERPEHCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 

       310        320        330        340        350        360 
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG 

       370        380        390        400        410        420 
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA 

       430        440        450        460        470        480 
QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM 

       490        500        510        520        530        540 
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS 

       550        560        570        580        590        600 
STELHSSEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 

       610        620        630        640        650        660 
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT 

       670        680        690        700        710        720 
NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE 

       730        740        750        760        770        780 
GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP 

       790        800        810        820        830        840 
GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW 

       850        860        870        880        890        900 
FPSNYVEEMI NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 

       910        920        930        940        950        960 
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC 

       970        980        990       1000       1010       1020 
RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS 

      1030       1040       1050       1060       1070       1080 
SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMAGGHC GYVLQPSTMR DEAFDPFDKS 

      1090       1100       1110       1120       1130       1140 
SLRGLEPCVI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW 

      1150       1160       1170       1180       1190       1200 
PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 

      1210       1220       1230       1240       1250       1260 
ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF 

      1270       1280       1290       1300 
RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC SL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[2]	"Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking." Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F. Biochem. J. 316:583-591(1996) [PubMed: 8687404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 846-1052. Tissue: Oocyte.
[3]	"Signal transduction by normal isoforms and W mutant variants of the Kit receptor tyrosine kinase." Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E., Bernstein A., Pawson T. EMBO J. 10:2451-2459(1991) [PubMed: 1714377] [Abstract] Cited for: INTERACTION WITH KIT, PHOSPHORYLATION.
[4]	"Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction." Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A. Mol. Cell. Biol. 11:3780-3785(1991) [PubMed: 1646396] [Abstract] Cited for: INTERACTION WITH PDGFRA, ACTIVATION BY PDGFRA.
[5]	"Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation." Bazenet C.E., Gelderloos J.A., Kazlauskas A. Mol. Cell. Biol. 16:6926-6936(1996) [PubMed: 8943348] [Abstract] Cited for: INTERACTION WITH PDGFRA.
[6]	"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma." Sawano A., Takahashi T., Yamaguchi S., Shibuya M. Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed: 9299537] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH FLT1.
[7]	"Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains." Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S. J. Biol. Chem. 275:16030-16036(2000) [PubMed: 10748127] [Abstract] Cited for: INTERACTION WITH KHDRBS1.
[8]	"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b." Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M. Nature 403:211-216(2000) [PubMed: 10646608] [Abstract] Cited for: INTERACTION WITH CBLB.
[9]	"MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT." Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D. J. Biol. Chem. 276:36043-36050(2001) [PubMed: 11463797] [Abstract] Cited for: INTERACTION WITH CLNK, DOMAIN.
[10]	"Mechanism of TrkB-mediated hippocampal long-term potentiation." Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M. Neuron 36:121-137(2002) [PubMed: 12367511] [Abstract] Cited for: INTERACTION WITH NTRK2.
[11]	"Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction." Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C., Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R., Gronski M., Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C., Penninger J.M. Immunity 21:167-177(2004) [PubMed: 15308098] [Abstract] Cited for: PHOSPHORYLATION, UBIQUITINATION, FUNCTION.
[12]	"Tyrosine 769 of the keratinocyte growth factor receptor is required for receptor signaling but not endocytosis." Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R. Biochem. Biophys. Res. Commun. 327:523-532(2005) [PubMed: 15629145] [Abstract] Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
[13]	"Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity." Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G. Exp. Mol. Med. 37:161-168(2005) [PubMed: 16000869] [Abstract] Cited for: INTERACTION WITH INPP5D.
[14]	"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: 17620338] [Abstract] Cited for: INTERACTION WITH PDGFRB.
[15]	"Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration." Sun Y., Ling K., Wagoner M.P., Anderson R.A. J. Cell Biol. 178:297-308(2007) [PubMed: 17635937] [Abstract] Cited for: INTERACTION WITH PIP5K1C.
[16]	"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: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, MASS SPECTROMETRY. Tissue: Mast cell.
[17]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-379; TYR-481; TYR-506 AND TYR-977, MASS SPECTROMETRY. Tissue: Brain.
[18]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248 AND SER-1263, MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"Themis controls thymocyte selection through regulation of T cell antigen receptor-mediated signaling." Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C., Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J., Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J. Nat. Immunol. 10:848-856(2009) [PubMed: 19597499] [Abstract] Cited for: INTERACTION WITH THEMIS.
[20]	"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling." Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P. J. Biol. Chem. 286:10918-10929(2011) [PubMed: 21262971] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC065091 mRNA. Translation: AAH65091.1. X95346 mRNA. Translation: CAA64639.1.
IPI	IPI00121089.
RefSeq	NP_067255.2. NM_021280.3.
UniGene	Mm.44463.
3D structure databases
ProteinModelPortal	Q62077.
SMR	Q62077. Positions 156-218, 345-384, 489-933, 1088-1195.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62077. 9 interactions.
MINT	MINT-124146.
STRING	Q62077.
PTM databases
PhosphoSite	Q62077.
Proteomic databases
PRIDE	Q62077.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
GeneID	18803.
KEGG	mmu:18803.
NMPDR	fig\|10090.3.peg.7332.
Organism-specific databases
CTD	5335.
MGI	MGI:97615. Plcg1.
Phylogenomic databases
HOGENOM	HBG402919.
HOVERGEN	HBG053611.
InParanoid	Q62077.
OMA	YRSLMYS.
OrthoDB	EOG4320X7.
PhylomeDB	Q62077.
Enzyme and pathway databases
BRENDA	3.1.4.11. 3474.
Gene expression databases
ArrayExpress	Q62077.
Bgee	Q62077.
CleanEx	MM_PLCG1.
Genevestigator	Q62077.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR011993. PH_type. IPR001192. Pinositol_PLipase_C. IPR016279. PLC-gamma. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR001849. Pleckstrin_homology. 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]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:2.30.29.30. PH_type. 3 hits. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits. G3DSA:3.30.505.10. SH2. 2 hits.
KO	K05859.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_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]
PIRSF	PIRSF000952. PLC-gamma. 1 hit.
PRINTS	PR00390. PHPHLIPASEC. PR00401. SH2DOMAIN. PR00452. SH3DOMAIN.
SMART	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]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	295106.
SOURCE	Search...

Entry information

Entry name

PLCG1_MOUSE

Accession

Primary (citable) accession number: Q62077
Secondary accession number(s): Q6P1G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents