Plcg2
entrez
234779
canonical
uniprot
Q8CIH5
canonical
ensembl
ENSMUSG00000034330
resolver
ensp
ENSMUSP00000079991
resolver
enst
ENSMUST00000081232
resolver
genesymbol
Plcg2
resolver
uniprot
Q3UBA8
resolver
uniprot
Q3UQT0
resolver
uniprot
Q8VE69
resolver
uniprot_entry
PLCG2_MOUSE
resolver
uniprot_sec
Q3UBA8
resolver
uniprot_sec
Q3UQT0
resolver
uniprot_sec
Q8VE69
resolver
amino_acid_sequence
MTTMVNVDTLPEYEKSQIKRALELGTVMTVFNARKSTPERRTVQMIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRHKAECCFTILYGTQFVLSTLSLATDSKEDAVKWLSGLKILHQEAMSASTPTMIESWLRKQIYSVDQTRRNSISLRELKTILPLVNFKVSGIKFLKDKLVEIGAQKDELSFEQFHLFYKKLMFDQQKSILDEFKKDSSVFILGNTDRPDASAVYLQDFQRFLLHEQQELWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENSIWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRAGCRCIELDCWDGPDGKPIIYHGWTRTTKIKFDDVVQAIRDHAFVTSSFPVILSIEEHCSVEQQRHMAKVFKEVLGDMLLTKPTEASADQLPSPSQLREKIIIKHKKLGPKGDVDVNVEDKKDEHKPQGELYMWDSIDQKWTRHYCAIADAKLSFGDDIEQAVEEEPVQDTPPTELHFGEKWFHKKVESRTSAEKLLQEYCAETGAKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMENGVMKYYLTDNLTFNSIYALIQHYREAHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDMLMRIPRDGAFLIRKREGTNSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYYEKHALYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDYKAKRSDELTFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISAGDAEEMEKQIIEDNPLGSLCKGILDLNTYNVVKAPQGKNQKAFVFILEPKKQGDPPVEFATDRVEELFEWFQSIREITWKMDTKENNMKYWERNQSIAIELSDLVVYCKPTSKTKDHLENPDFREIRSFVETKADSIVRQKPVDLLRYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTPDKYMQMNHALFSLNGRTGYVLQPESMRSEKYDPMPLESQRKILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDSNKFKTTVVNDNGLSPVWAPTQEKVTFEIYDPNLAFLRFVVYEEDMFSDPNFLAHATYPIKGIKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSCRQLRRRQEELNNQLFLYDTHQNLRGANRDALVKEFNVNENQLQLYQEKCNRRLREKRVSNSRFYS
uniprot
proteins
ec_number
3.1.4.11
uniprot
proteins
function
FUNCTION: 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. {ECO:0000250|UniProtKB:P16885}.
uniprot
proteins
mass_dalton
147592
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:P16885, ECO:0000269|PubMed:9312046}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23478294
uniprot
proteins
pubmed
27992403
uniprot
proteins
pubmed
9312046
uniprot
proteins
sequence_length
1265
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:23478294}.
uniprot
proteins